From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2goy.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2goy.jpg|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2goy| PDB=2goy | SCENE= }} | | {{STRUCTURE_2goy| PDB=2goy | SCENE= }} |
| | | | |
| - | '''Crystal structure of assimilatory adenosine 5'-phosphosulfate reductase with bound APS'''
| + | ===Crystal structure of assimilatory adenosine 5'-phosphosulfate reductase with bound APS=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | APS reductase catalyzes the first committed step of reductive sulfate assimilation in pathogenic bacteria, including Mycobacterium tuberculosis, and is a promising target for drug development. We report the 2.7 A resolution crystal structure of Pseudomonas aeruginosa APS reductase in the thiosulfonate intermediate form of the catalytic cycle and with substrate bound. The structure, high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry, and quantitative kinetic analysis, establish that the two chemically discrete steps of the overall reaction take place at distinct sites on the enzyme, mediated via conformational flexibility of the C-terminal 18 residues. The results address the mechanism by which sulfonucleotide reductases protect the covalent but labile enzyme-intermediate before release of sulfite by the protein cofactor thioredoxin. P. aeruginosa APS reductase contains an [4Fe-4S] cluster that is essential for catalysis. The structure reveals an unusual mode of cluster coordination by tandem cysteine residues and suggests how this arrangement might facilitate conformational change and cluster interaction with the substrate. Assimilatory 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductases are evolutionarily related, homologous enzymes that catalyze the same overall reaction, but do so in the absence of an [Fe-S] cluster. The APS reductase structure reveals adaptive use of a phosphate-binding loop for recognition of the APS O3' hydroxyl group, or the PAPS 3'-phosphate group.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17010373}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17010373 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17010373}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Nucleotide binding]] | | [[Category: Nucleotide binding]] |
| | [[Category: Thiosulfonate intermediate]] | | [[Category: Thiosulfonate intermediate]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:21:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:14:47 2008'' |
Revision as of 15:14, 28 July 2008
Template:STRUCTURE 2goy
Crystal structure of assimilatory adenosine 5'-phosphosulfate reductase with bound APS
Template:ABSTRACT PUBMED 17010373
About this Structure
2GOY is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase., Chartron J, Carroll KS, Shiau C, Gao H, Leary JA, Bertozzi CR, Stout CD, J Mol Biol. 2006 Nov 24;364(2):152-69. Epub 2006 Sep 1. PMID:17010373
Page seeded by OCA on Mon Jul 28 18:14:47 2008
